Rabbit anti-Human DDOST Polyclonal Antibody

Uniprot Id

P39656

Target Species

Human

Target Name

DDOST

Target Full Name

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit

Target Function

Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Required for the assembly of both SST3A- and SS3B-containing OST complexes. Required for efficient N-glycosylation.; Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Required for the assembly of both SST3A- and SS3B-containing OST complexes.

Target Involvement

Congenital disorder of glycosylation 1R (CDG1R)

Target Subcellular Location

Endoplasmic reticulum membrane; Single-pass type I membrane protein.

Target Protein Families

DDOST 48 kDa subunit family

Target Synonyms

DDOST; KIAA0115; OST48; OK/SW-cl.45; Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit; DDOST 48 kDa subunit; Oligosaccharyl transferase 48 kDa subunit

Target Background

This gene encodes a component of the oligosaccharyltransferase complex which catalyzes the transfer of high-mannose oligosaccharides to asparagine residues on nascent polypeptides in the lumen of the rough endoplasmic reticulum. The protein complex co-purifies with ribosomes. The product of this gene is also implicated in the processing of advanced glycation endproducts (AGEs), which form from non-enzymatic reactions between sugars and proteins or lipids and are associated with aging and hyperglycemia.